Antimicrobial Activity of Chitin

C Antimicrobial Activity of Chitin, Chitosan, and Their Oligosaccharides... 

A number of important papers could not be cited in this chapter, due to the length limitations and the specific target of the chapter. For example, the antimicrobial activity of chitosans [349], the chitinolytic enzymes, the preparation of cosmetics, and the occurrence of chitin in fungi [350] are some of the subjects not dealt with specifically here, notwithstanding their importance. 

Tsai, G.J., Su, W.-H., Chen, H.C., and Pan, C.-L. 2002. Antimicrobial activity of shrimp chitin and chitosan from different treatments and applications of fish preservation. Fisheries Sci. 68, 170-177. 

Yalpani, M., Johnson, F., and Robinson, L.E. 1992. Antimicrobial activity of some chitosan derivatives. In Advances in Chitin and Chitosan (C J. Brine, P.A. Sandford, and J.P. Zikakis, eds), pp. 543-555. Elsevier Applied Science, London, UK. 

Peculiar characteristics of chitins and chitosans are hemostatic action, anti-inflammatory effect, biodegradability, biocompatibihty, besides antimicrobial activity, retention of growth factors, release of glucosamine and M-acetylglucosamine monomers and oligomers, and stimulation of cellular activities [11,12,295-297]. 

The arsenal of plant defense peptides contains members capable of binding carbohydrate residues, namely /31-4 linked A -acetyl glucosamine residues that form the biopolymer chitin. The actual mode of action remains unclear. Antifungal and antimicrobial activity has been shown in vitro. For example Ac-AMP2 is a small disulfide-rich chitin-binding peptide isolated from the seeds of Amaranthus caudatus with antimicrobial activity. It differs from Ac-AMP 1 by one additional arginine residue at the C-terminus. The structure was determined by NMR and contains a cystine knot motif. Ac-AMP2 displays a so-called hevein domain partly... 

Chen et al. (2008) have expressed a codon-optimized form of the CM4 peptide in E. coli. In this case, two alternative expression/purification systems were examined namely the widely used glutathione-S-transferase (GST) and a chitin-binding domain (CBD) system with associated intein splicing (New England Biolabs Inc.). The GST system failed to allow recovery of expressed fusion protein. In contrast, the CBD/intein system allowed the recovery of 110 mg/L fusion protein with a final RP-HPLC purification step yielding 2.1 mg/L of pure peptide which displayed antimicrobial activity against E. coli Ki2D3i and Salmonella. 

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